CATH Classification
Level | CATH Code | Description |
---|---|---|
1 | Mainly Alpha | |
1.10 | Orthogonal Bundle | |
1.10.620 | Ribonucleotide Reductase, subunit A | |
1.10.620.20 | Ribonucleotide Reductase, subunit A |
Domain Context
CATH Clusters
Superfamily | Ribonucleotide Reductase, subunit A |
Functional Family | Ribonucleoside-diphosphate reductase subunit M2 B |
Enzyme Information
1.17.4.1 |
Ribonucleoside-diphosphate reductase.
based on mapping to UniProt P31350
2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H(2)O = ribonucleoside diphosphate + thioredoxin.
-!- This enzyme is responsible for the de novo conversion of ribonucleoside diphosphates into deoxyribonucleoside diphosphates, which are essential for DNA synthesis and repair. -!- There are three types of this enzyme differing in their cofactors. -!- Class Ia enzymes contain a diiron(III)-tyrosyl radical, class Ib enzymes contain a dimanganese-tyrosyl radical, and class II enzymes contain adenosylcobalamin. -!- In all cases the cofactors are involved in generation of a transient thiyl (sulfanyl) radical on a cysteine residue, which attacks the substrate, forming a ribonucleotide 3'-radical, followed by water loss to form a ketyl (alpha-oxoalkyl) radical. -!- The ketyl radical is reduced to 3'-keto-deoxynucleotide concomitant with formation of a disulfide anion radical between two cysteine residues. -!- A proton-coupled electron-transfer from the disulfide radical to the substrate generates a 3'-deoxynucleotide radical, and the the final product is formed when the hydrogen atom that was initially removed from the 3'-position of the nucleotide by the thiyl radical is returned to the same position. -!- The disulfide bridge is reduced by the action of thioredoxin. -!- Cf. EC 1.1.98.6 and EC 1.17.4.2.
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UniProtKB Entries (1)
P31350 |
RIR2_HUMAN
Homo sapiens
Ribonucleoside-diphosphate reductase subunit M2
|
PDB Structure
PDB | 3VPO |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | |
Primary Citation |
Essential role of E106 in the proton-coupled electron transfer in human
to be published
|